摘要
M型相关瞬时受体电位通道6和7 (TRPM6和TRPM7)是特有的在C端有激酶结构域的阳离子通路。跨膜孔隙和激酶都具有功能,并已通过实验确定了它们的特性。但是否是一个结构域调节其他区域的功能或反之还不清楚。这些蛋白质在镁稳态和包括细胞死亡、增殖、分化和迁移的其它细胞过程中发挥重要生理作用,并与多种病症有关。最近,对表现TRM7激酶死亡突变的小鼠的研究表明,该酶是紧张环境中镁离子传感器和转换器的部件。此外,TRPM7的激酶可以作用于其自身的染色质重塑过程。如此,最近该领域的研究工作提供了对这些受关注的蛋白质的功能的新理解及其与疾病的关系。
关键词: α-激酶,染色质重塑,Mg2+体内平衡,Mg2+传感,转录因子,TRPM通路。
Current Medicinal Chemistry
Title:The Different Roles of The Channel-Kinases TRPM6 and TRPM7
Volume: 22 Issue: 25
Author(s): Deny Cabezas-Bratesco, Sebastian Brauchi, Vicente Gonzalez-Teuber, Ximena Steinberg, Ignacio Valencia and Charlotte Colenso
Affiliation:
关键词: α-激酶,染色质重塑,Mg2+体内平衡,Mg2+传感,转录因子,TRPM通路。
摘要: Melastatin-related Transient Receptor Potential 6 and 7 (TRPM6 and TRPM7) are cation channels with the almost unique trait of each possessing a kinase domain in its C terminus. Both the transmembrane pore and kinase are functional, and have been characterized experimentally, but whether one domain regulates the function of the other, or vice versa has remained largely unsettled. These proteins play important physiological roles in magnesium homeostasis and other cellular processes such as cell death, proliferation, differentiation and migration, and are consequently associated with several types of pathologies. Recently, studies performed in mice expressing a TRPM7 kinase-dead mutant suggest that the enzyme may function as part of a Mg2+ sensor and transducer of signaling pathways during stressful environmental conditions. Additionally, it has been shown that TRPM7's kinase can act on its own in chromatin remodeling processes. Thus, the recent work in this field has provided new insights into the function of these interesting proteins and how they might be involved in human disease.
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Deny Cabezas-Bratesco, Sebastian Brauchi, Vicente Gonzalez-Teuber, Ximena Steinberg, Ignacio Valencia and Charlotte Colenso , The Different Roles of The Channel-Kinases TRPM6 and TRPM7, Current Medicinal Chemistry 2015; 22 (25) . https://dx.doi.org/10.2174/0929867322666150716115644
DOI https://dx.doi.org/10.2174/0929867322666150716115644 |
Print ISSN 0929-8673 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-533X |
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